ID   PLAK_MOUSE              Reviewed;         745 AA.
AC   Q02257; Q8CGD3;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 3.
DT   16-NOV-2011, entry version 102.
DE   RecName: Full=Junction plakoglobin;
DE   AltName: Full=Desmoplakin III;
DE   AltName: Full=Desmoplakin-3;
GN   Name=Jup;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 125-745.
RX   MEDLINE=92376536; PubMed=1509266; DOI=10.1126/science.257.5073.1142-a;
RA   Butz S., Stappert J., Weissig H., Kemler R.;
RT   "Plakoglobin and beta-catenin: distinct but closely related.";
RL   Science 257:1142-1144(1992).
RN   [4]
RP   SEQUENCE REVISION TO 418 AND 420.
RA   Butz S.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA   Butz S., Kemler R.;
RT   "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT   adhesion.";
RL   FEBS Lett. 355:195-200(1994).
RN   [6]
RP   RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP   ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA   Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT   "Deconstructing the cadherin-catenin-actin complex.";
RL   Cell 123:889-901(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=19015309; DOI=10.1084/jem.20080406;
RA   Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R.,
RA   Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O.,
RA   Bixel M.G., Butz S., Vestweber D.;
RT   "VE-PTP maintains the endothelial barrier via plakoglobin and becomes
RT   dissociated from VE-cadherin by leukocytes and by VEGF.";
RL   J. Exp. Med. 205:2929-2945(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Common junctional plaque protein. The membrane-
CC       associated plaques are architectural elements in an important
CC       strategic position to influence the arrangement and function of
CC       both the cytoskeleton and the cells within the tissue. The
CC       presence of plakoglobin in both the desmosomes and in the
CC       intermediate junctions suggests that it plays a central role in
CC       the structure and function of submembranous plaques. Acts as a
CC       substrate for VE-PTP and is required by it to stimulate VE-
CC       cadherin function in endothelial cells. Can replace beta-catenin
CC       in E-cadherin/catenin adhesion complexes which are proposed to
CC       couple cadherins to the actin cytoskeleton.
CC   -!- SUBUNIT: Homodimer. Component of an E-cadherin/ catenin adhesion
CC       complex composed of at least E-cadherin/CDH1 and gamma-
CC       catenin/JUP, and possibly alpha-catenin/CTNNA1; the complex is
CC       located to adherens junctions. The stable association of CTNNA1 is
CC       controversial as CTNNA1 was shown not to bind to F-actin when
CC       assembled in the complex. Interacts with MUC1. Interacts with
CC       CAV1. Interacts with PTPRJ (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell
CC       junction, desmosome. Cytoplasm, cytoskeleton. Membrane; Peripheral
CC       membrane protein. Note=Cytoplasmic in a soluble and membrane-
CC       associated form.
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 9 ARM repeats.
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DR   EMBL; AK170934; BAE42126.1; -; mRNA.
DR   EMBL; BC040757; AAH40757.1; -; mRNA.
DR   EMBL; BC094461; AAH94461.1; -; mRNA.
DR   EMBL; M90365; AAB02885.1; -; mRNA.
DR   IPI; IPI00229475; -.
DR   PIR; S35092; S35092.
DR   RefSeq; NP_034723.1; NM_010593.2.
DR   UniGene; Mm.299774; -.
DR   ProteinModelPortal; Q02257; -.
DR   SMR; Q02257; 111-673.
DR   IntAct; Q02257; 4.
DR   STRING; Q02257; -.
DR   PhosphoSite; Q02257; -.
DR   PRIDE; Q02257; -.
DR   Ensembl; ENSMUST00000001592; ENSMUSP00000001592; ENSMUSG00000001552.
DR   Ensembl; ENSMUST00000107403; ENSMUSP00000103026; ENSMUSG00000001552.
DR   GeneID; 16480; -.
DR   KEGG; mmu:16480; -.
DR   CTD; 3728; -.
DR   MGI; MGI:96650; Jup.
DR   GeneTree; ENSGT00570000078959; -.
DR   HOGENOM; HBG357527; -.
DR   HOVERGEN; HBG000919; -.
DR   InParanoid; Q02257; -.
DR   OMA; DDMDATY; -.
DR   OrthoDB; EOG4FR0R3; -.
DR   PhylomeDB; Q02257; -.
DR   NextBio; 289775; -.
DR   ArrayExpress; Q02257; -.
DR   Bgee; Q02257; -.
DR   CleanEx; MM_JUP; -.
DR   Genevestigator; Q02257; -.
DR   GermOnline; ENSMUSG00000001552; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:RefGenome.
DR   GO; GO:0034747; C:Axin-APC-beta-catenin-GSK3B complex; IBA:RefGenome.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:RefGenome.
DR   GO; GO:0016342; C:catenin complex; IBA:RefGenome.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0030057; C:desmosome; IDA:MGI.
DR   GO; GO:0005916; C:fascia adherens; IBA:RefGenome.
DR   GO; GO:0009898; C:internal side of plasma membrane; IBA:RefGenome.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005915; C:zonula adherens; IBA:RefGenome.
DR   GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
DR   GO; GO:0045296; F:cadherin binding; IBA:RefGenome.
DR   GO; GO:0019901; F:protein kinase binding; IBA:RefGenome.
DR   GO; GO:0042153; F:RPTP-like protein binding; IPI:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IBA:RefGenome.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:RefGenome.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; IBA:RefGenome.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:RefGenome.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IBA:RefGenome.
DR   GO; GO:0002159; P:desmosome assembly; IMP:MGI.
DR   GO; GO:0007398; P:ectoderm development; IBA:RefGenome.
DR   GO; GO:0007369; P:gastrulation; IBA:RefGenome.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IBA:RefGenome.
DR   GO; GO:0003136; P:negative regulation of heart induction by canonical Wnt receptor signaling pathway; IBA:RefGenome.
DR   GO; GO:0003308; P:negative regulation of Wnt receptor signaling pathway involved in heart development; IBA:RefGenome.
DR   GO; GO:0007399; P:nervous system development; IBA:RefGenome.
DR   GO; GO:0048599; P:oocyte development; IBA:RefGenome.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:RefGenome.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR013284; Beta-catenin.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   KO; K10056; -.
DR   Pfam; PF00514; Arm; 4.
DR   PRINTS; PR01869; BCATNINFAMLY.
DR   SMART; SM00185; ARM; 12.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 9.
PE   1: Evidence at protein level;
KW   Acetylation; Cell adhesion; Cell junction; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN         1    745       Junction plakoglobin.
FT                                /FTId=PRO_0000064279.
FT   REPEAT      132    171       ARM 1.
FT   REPEAT      216    255       ARM 2.
FT   REPEAT      258    297       ARM 3.
FT   REPEAT      342    381       ARM 4.
FT   REPEAT      383    420       ARM 5.
FT   REPEAT      423    464       ARM 6.
FT   REPEAT      470    510       ARM 7.
FT   REPEAT      512    551       ARM 8.
FT   REPEAT      574    613       ARM 9.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      20     20       Phosphotyrosine (By similarity).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphotyrosine (By similarity).
FT   MOD_RES     665    665       Phosphoserine.
SQ   SEQUENCE   745 AA;  81801 MW;  9609619D94052FC5 CRC64;
     MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GIMDEDDACG RQYTLKKTTT
     YTQGVPQNQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL LLATQVEGQT TNLQRLAEPS
     QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM
     GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE
     SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ
     ESKLIILANG GPQGLVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE AGGMQALGKH
     LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL SVDDVNVLTC ATGTLSNLTC
     NNSKNKTLVT QNSGVEALIH AILRAGDKDD ITEPAVCALR HLTSRHPEAE MAQNSVRLNY
     GIPAIVKLLN QPNQWPLVKA TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR
     HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI
     QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF RISEDKNPDY
     RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT YRPMYSSDVP LDPLDMHMDL
     DGDYPMDTYS DGLRPPYPTA DHMLA
//